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P05042

- FUMC_ECOLI

UniProt

P05042 - FUMC_ECOLI

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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the reversible addition of water to fumarate to give L-malate.1 Publication

Catalytic activityi

(S)-malate = fumarate + H2O.1 Publication

Enzyme regulationi

Inhibited by ATP and S-2,3-dicarboxyaziridine.1 Publication

Kineticsi

  1. KM=50 µM for L-malate (at pH 7.3 and 30 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 8.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei188 – 1881Proton donor/acceptorBy similarity
Active sitei318 – 3181By similarity
Binding sitei319 – 3191SubstrateBy similarity
Sitei331 – 3311Important for catalytic activity

GO - Molecular functioni

  1. fumarate hydratase activity Source: EcoCyc

GO - Biological processi

  1. fumarate metabolic process Source: InterPro
  2. response to oxidative stress Source: EcoCyc
  3. tricarboxylic acid cycle Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

BioCyciEcoCyc:FUMC-MONOMER.
ECOL316407:JW1603-MONOMER.
MetaCyc:FUMC-MONOMER.
SABIO-RKP05042.
UniPathwayiUPA00223; UER01007.

Names & Taxonomyi

Protein namesi
Recommended name:
Fumarate hydratase class II (EC:4.2.1.2)
Short name:
Fumarase C
Alternative name(s):
Iron-independent fumarase
Gene namesi
Name:fumC
Ordered Locus Names:b1611, JW1603
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10358. fumC.

Subcellular locationi

GO - Cellular componenti

  1. tricarboxylic acid cycle enzyme complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi126 – 1261R → A: Reduces enzyme activity 10-fold. 1 Publication
Mutagenesisi127 – 1271K → D: No effect. 1 Publication
Mutagenesisi129 – 1291H → N: No effect on activity, but the carboxyamide group from Asn129 swings into the B site and replaces S-malate by forming a bifurcated hydrogen bond with Asn131 and Asp132. 2 Publications
Mutagenesisi188 – 1881H → N: Reduces activity 200-fold. 1 Publication
Mutagenesisi315 – 3151E → Q: Reduces activity 10-fold. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 467467Fumarate hydratase class IIPRO_0000161275Add
BLAST

Proteomic databases

PaxDbiP05042.
PRIDEiP05042.

Expressioni

Inductioni

Under conditions of iron limitation and oxidative stress.1 Publication

Gene expression databases

GenevestigatoriP05042.

Interactioni

Subunit structurei

Homotetramer.6 Publications

Protein-protein interaction databases

DIPiDIP-9719N.
IntActiP05042. 14 interactions.
STRINGi511145.b1611.

Structurei

Secondary structure

1
467
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 95
Beta strandi12 – 165
Helixi24 – 329
Helixi42 – 6120
Helixi67 – 8115
Turni82 – 854
Helixi86 – 883
Beta strandi92 – 954
Helixi100 – 11718
Helixi130 – 1345
Turni135 – 1373
Helixi140 – 15819
Helixi160 – 17718
Turni178 – 1803
Beta strandi182 – 1876
Beta strandi190 – 1967
Helixi197 – 22226
Turni230 – 2323
Helixi242 – 25413
Helixi264 – 2696
Helixi272 – 29827
Beta strandi302 – 3054
Beta strandi308 – 3103
Helixi328 – 35225
Helixi362 – 38625
Helixi388 – 3903
Helixi395 – 40410
Helixi406 – 4083
Helixi409 – 4135
Turni414 – 4163
Helixi418 – 43114
Helixi435 – 4417
Helixi447 – 4537
Helixi456 – 4583

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FUOX-ray1.98A/B1-467[»]
1FUPX-ray2.30A/B1-467[»]
1FUQX-ray2.00A/B1-467[»]
1FURX-ray1.95A/B1-467[»]
1KQ7X-ray2.60A/B1-467[»]
1YFEX-ray2.19A1-467[»]
2FUSX-ray2.20A/B1-467[»]
ProteinModelPortaliP05042.
SMRiP05042. Positions 4-459.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05042.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni98 – 1003Substrate binding
Regioni129 – 1324B site
Regioni139 – 1413Substrate binding
Regioni187 – 1882Substrate bindingBy similarity
Regioni324 – 3263Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0114.
HOGENOMiHOG000061736.
InParanoidiP05042.
KOiK01679.
OMAiMESFNIH.
OrthoDBiEOG6V1M4M.
PhylomeDBiP05042.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
HAMAPiMF_00743. FumaraseC.
InterProiIPR005677. Fum_hydII.
IPR024083. Fumarase/histidase_N.
IPR018951. Fumarase_C_C.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
[Graphical view]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PfamiPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00979. fumC_II. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P05042-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNTVRSEKDS MGAIDVPADK LWGAQTQRSL EHFRISTEKM PTSLIHALAL
60 70 80 90 100
TKRAAAKVNE DLGLLSEEKA SAIRQAADEV LAGQHDDEFP LAIWQTGSGT
110 120 130 140 150
QSNMNMNEVL ANRASELLGG VRGMERKVHP NDDVNKSQSS NDVFPTAMHV
160 170 180 190 200
AALLALRKQL IPQLKTLTQT LNEKSRAFAD IVKIGRTHLQ DATPLTLGQE
210 220 230 240 250
ISGWVAMLEH NLKHIEYSLP HVAELALGGT AVGTGLNTHP EYARRVADEL
260 270 280 290 300
AVITCAPFVT APNKFEALAT CDALVQAHGA LKGLAASLMK IANDVRWLAS
310 320 330 340 350
GPRCGIGEIS IPENEPGSSI MPGKVNPTQC EALTMLCCQV MGNDVAINMG
360 370 380 390 400
GASGNFELNV FRPMVIHNFL QSVRLLADGM ESFNKHCAVG IEPNRERINQ
410 420 430 440 450
LLNESLMLVT ALNTHIGYDK AAEIAKKAHK EGLTLKAAAL ALGYLSEAEF
460
DSWVRPEQMV GSMKAGR
Length:467
Mass (Da):50,489
Last modified:August 13, 1987 - v1
Checksum:i3D67E3C0F0FDF40B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X04065 Genomic DNA. Translation: CAA27698.1.
U00096 Genomic DNA. Translation: AAC74683.1.
AP009048 Genomic DNA. Translation: BAA15349.1.
X00522 Genomic DNA. Translation: CAA25205.1.
PIRiS07138. UFEC.
RefSeqiNP_416128.1. NC_000913.3.
YP_489874.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74683; AAC74683; b1611.
BAA15349; BAA15349; BAA15349.
GeneIDi12934129.
946147.
KEGGiecj:Y75_p1587.
eco:b1611.
PATRICi32118524. VBIEscCol129921_1682.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X04065 Genomic DNA. Translation: CAA27698.1 .
U00096 Genomic DNA. Translation: AAC74683.1 .
AP009048 Genomic DNA. Translation: BAA15349.1 .
X00522 Genomic DNA. Translation: CAA25205.1 .
PIRi S07138. UFEC.
RefSeqi NP_416128.1. NC_000913.3.
YP_489874.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FUO X-ray 1.98 A/B 1-467 [» ]
1FUP X-ray 2.30 A/B 1-467 [» ]
1FUQ X-ray 2.00 A/B 1-467 [» ]
1FUR X-ray 1.95 A/B 1-467 [» ]
1KQ7 X-ray 2.60 A/B 1-467 [» ]
1YFE X-ray 2.19 A 1-467 [» ]
2FUS X-ray 2.20 A/B 1-467 [» ]
ProteinModelPortali P05042.
SMRi P05042. Positions 4-459.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-9719N.
IntActi P05042. 14 interactions.
STRINGi 511145.b1611.

Proteomic databases

PaxDbi P05042.
PRIDEi P05042.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74683 ; AAC74683 ; b1611 .
BAA15349 ; BAA15349 ; BAA15349 .
GeneIDi 12934129.
946147.
KEGGi ecj:Y75_p1587.
eco:b1611.
PATRICi 32118524. VBIEscCol129921_1682.

Organism-specific databases

EchoBASEi EB0353.
EcoGenei EG10358. fumC.

Phylogenomic databases

eggNOGi COG0114.
HOGENOMi HOG000061736.
InParanoidi P05042.
KOi K01679.
OMAi MESFNIH.
OrthoDBi EOG6V1M4M.
PhylomeDBi P05042.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci EcoCyc:FUMC-MONOMER.
ECOL316407:JW1603-MONOMER.
MetaCyc:FUMC-MONOMER.
SABIO-RK P05042.

Miscellaneous databases

EvolutionaryTracei P05042.
PROi P05042.

Gene expression databases

Genevestigatori P05042.

Family and domain databases

Gene3Di 1.10.275.10. 1 hit.
HAMAPi MF_00743. FumaraseC.
InterProi IPR005677. Fum_hydII.
IPR024083. Fumarase/histidase_N.
IPR018951. Fumarase_C_C.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
[Graphical view ]
PANTHERi PTHR11444. PTHR11444. 1 hit.
Pfami PF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view ]
PRINTSi PR00149. FUMRATELYASE.
SUPFAMi SSF48557. SSF48557. 1 hit.
TIGRFAMsi TIGR00979. fumC_II. 1 hit.
PROSITEi PS00163. FUMARATE_LYASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structural and functional relationships between fumarase and aspartase. Nucleotide sequences of the fumarase (fumC) and aspartase (aspA) genes of Escherichia coli K12."
    Woods S.A., Miles J.S., Roberts R.E., Guest J.R.
    Biochem. J. 237:547-557(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Complete nucleotide sequence of the fumarase gene fumA, of Escherichia coli."
    Miles J.S., Guest J.R.
    Nucleic Acids Res. 12:3631-3642(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-89.
  6. "The fumarase genes of Escherichia coli: location of the fumB gene and discovery of a new gene (fumC)."
    Guest J.R., Miles J.S., Roberts R.E., Woods S.A.
    J. Gen. Microbiol. 131:2971-2984(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-89.
  7. "Purification and characterization of two types of fumarase from Escherichia coli."
    Ueda Y., Yumoto N., Tokushige M., Fukui K., Ohya-Nishiguchi H.
    J. Biochem. 109:728-733(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-20, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT.
  8. "Purification and crystallization of fumarase C from Escherichia coli."
    Weaver T.M., Levitt D.G., Banaszak L.J.
    J. Mol. Biol. 231:141-144(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-15, SUBUNIT.
  9. "Two biochemically distinct classes of fumarase in Escherichia coli."
    Woods S.A., Shwartzbach S.D., Guest J.R.
    Biochim. Biophys. Acta 954:14-26(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOCHEMICAL ANALYSIS OF FUMA AND FUMC, SUBUNIT.
  10. "Oxygen, iron, carbon, and superoxide control of the fumarase fumA and fumC genes of Escherichia coli: role of the arcA, fnr, and soxR gene products."
    Park S.J., Gunsalus R.P.
    J. Bacteriol. 177:6255-6262(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  11. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  12. "The role of the allosteric B site in the fumarase reaction."
    Rose I.A., Weaver T.M.
    Proc. Natl. Acad. Sci. U.S.A. 101:3393-3397(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ARG-126; LYS-127 AND HIS-129.
  13. "Aspartase/fumarase superfamily: a common catalytic strategy involving general base-catalyzed formation of a highly stabilized aci-carboxylate intermediate."
    Puthan Veetil V., Fibriansah G., Raj H., Thunnissen A.M., Poelarends G.J.
    Biochemistry 51:4237-4243(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: REACTION MECHANISM.
  14. "Crystallographic studies of the catalytic and a second site in fumarase C from Escherichia coli."
    Weaver T., Banaszak L.
    Biochemistry 35:13955-13965(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), SUBUNIT.
  15. "Mutations of fumarase that distinguish between the active site and a nearby dicarboxylic acid binding site."
    Weaver T., Lees M., Banaszak L.
    Protein Sci. 6:834-842(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF MUTANTS ASN-129 AND ASN-188 IN COMPLEX WITH MALATE AND CITRATE, MUTAGENESIS OF HIS-129 AND HIS-188.
  16. "X-ray crystallographic and kinetic correlation of a clinically observed human fumarase mutation."
    Estevez M., Skarda J., Spencer J., Banaszak L., Weaver T.M.
    Protein Sci. 11:1552-1557(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF MUTANT GLN-315, MUTAGENESIS OF GLU-315, SUBUNIT.
  17. "Structure of free fumarase C from Escherichia coli."
    Weaver T.
    Acta Crystallogr. D 61:1395-1401(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS).

Entry informationi

Entry nameiFUMC_ECOLI
AccessioniPrimary (citable) accession number: P05042
Secondary accession number(s): P76891
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: October 29, 2014
This is version 149 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

There are 2 substrate-binding sites: the catalytic A site, and the non-catalytic B site that may play a role in the transfer of substrate or product between the active site and the solvent. Alternatively, the B site may bind allosteric effectors.

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3